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MPCP_YEAST
ID   MPCP_YEAST              Reviewed;         311 AA.
AC   P23641; D6VWP7;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 203.
DE   RecName: Full=Mitochondrial phosphate carrier protein;
DE   AltName: Full=Mitochondrial import receptor;
DE   AltName: Full=Phosphate transport protein;
DE            Short=PTP;
DE   AltName: Full=mPic 1;
DE   AltName: Full=p32;
DE   Contains:
DE     RecName: Full=Mitochondrial phosphate carrier protein, N-terminally processed;
GN   Name=MIR1; OrderedLocusNames=YJR077C; ORFNames=J1837;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-27.
RX   PubMed=2170848; DOI=10.1038/347488a0;
RA   Murakami H., Blobel G., Pain D.;
RT   "Isolation and characterization of the gene for a yeast mitochondrial
RT   import receptor.";
RL   Nature 347:488-491(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1840493; DOI=10.1021/bi00215a035;
RA   Phelps A., Schobert C.T., Wohlrab H.;
RT   "Cloning and characterization of the mitochondrial phosphate transport
RT   protein gene from the yeast Saccharomyces cerevisiae.";
RL   Biochemistry 30:248-252(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8840504;
RX   DOI=10.1002/(sici)1097-0061(199607)12:9<869::aid-yea964>3.0.co;2-1;
RA   Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT   "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading
RT   frames and a gene cluster with a counterpart on chromosome XI.";
RL   Yeast 12:869-875(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-4 AND SER-145, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP   SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   STRAIN=ATCC 76625 / YPH499;
RX   PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
RA   Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
RA   van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
RT   "Profiling phosphoproteins of yeast mitochondria reveals a role of
RT   phosphorylation in assembly of the ATP synthase.";
RL   Mol. Cell. Proteomics 6:1896-1906(2007).
CC   -!- FUNCTION: Transport of phosphate groups from the cytosol to the
CC       mitochondrial matrix.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000305}.
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DR   EMBL; X57478; CAA40716.1; -; Genomic_DNA.
DR   EMBL; M54879; AAA34782.1; -; Genomic_DNA.
DR   EMBL; Z49577; CAA89605.1; -; Genomic_DNA.
DR   EMBL; L47993; AAB39302.1; -; Genomic_DNA.
DR   EMBL; AY557913; AAS56239.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08863.1; -; Genomic_DNA.
DR   PIR; S12318; S12318.
DR   RefSeq; NP_012611.1; NM_001181735.1.
DR   AlphaFoldDB; P23641; -.
DR   SMR; P23641; -.
DR   BioGRID; 33833; 249.
DR   DIP; DIP-1714N; -.
DR   IntAct; P23641; 92.
DR   MINT; P23641; -.
DR   STRING; 4932.YJR077C; -.
DR   TCDB; 2.A.29.4.3; the mitochondrial carrier (mc) family.
DR   iPTMnet; P23641; -.
DR   MaxQB; P23641; -.
DR   PaxDb; P23641; -.
DR   PRIDE; P23641; -.
DR   EnsemblFungi; YJR077C_mRNA; YJR077C; YJR077C.
DR   GeneID; 853540; -.
DR   KEGG; sce:YJR077C; -.
DR   SGD; S000003838; MIR1.
DR   VEuPathDB; FungiDB:YJR077C; -.
DR   eggNOG; KOG0767; Eukaryota.
DR   HOGENOM; CLU_039456_1_0_1; -.
DR   InParanoid; P23641; -.
DR   OMA; VKIQTVP; -.
DR   BioCyc; MetaCyc:G3O-31707-MON; -.
DR   BioCyc; YEAST:G3O-31707-MON; -.
DR   PRO; PR:P23641; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P23641; protein.
DR   GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:SGD.
DR   GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; IPI:SGD.
DR   GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IDA:SGD.
DR   GO; GO:1990547; P:mitochondrial phosphate ion transmembrane transport; IEA:InterPro.
DR   GO; GO:0035435; P:phosphate ion transmembrane transport; IDA:SGD.
DR   Gene3D; 1.50.40.10; -; 1.
DR   InterPro; IPR002067; Mit_carrier.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   InterPro; IPR044677; Pic2/Mir1-like.
DR   PANTHER; PTHR45671; PTHR45671; 1.
DR   Pfam; PF00153; Mito_carr; 3.
DR   PRINTS; PR00926; MITOCARRIER.
DR   SUPFAM; SSF103506; SSF103506; 1.
DR   PROSITE; PS50920; SOLCAR; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Phosphoprotein; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..311
FT                   /note="Mitochondrial phosphate carrier protein"
FT                   /id="PRO_0000090635"
FT   INIT_MET        1
FT                   /note="Removed; alternate"
FT                   /evidence="ECO:0007744|PubMed:17761666"
FT   CHAIN           2..311
FT                   /note="Mitochondrial phosphate carrier protein, N-
FT                   terminally processed"
FT                   /id="PRO_0000423225"
FT   TOPO_DOM        1..19
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        20..40
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        41..62
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        63..83
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        84..115
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        137..165
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        187..214
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        215..235
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        236..253
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        254..274
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        275..311
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REPEAT          15..100
FT                   /note="Solcar 1"
FT   REPEAT          114..197
FT                   /note="Solcar 2"
FT   REPEAT          212..297
FT                   /note="Solcar 3"
FT   MOD_RES         2
FT                   /note="N-acetylserine; in Mitochondrial phosphate carrier
FT                   protein, N-terminally processed"
FT                   /evidence="ECO:0007744|PubMed:17761666"
FT   MOD_RES         4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17761666"
FT   MOD_RES         145
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17761666"
FT   CONFLICT        2
FT                   /note="S -> Y (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   311 AA;  32812 MW;  89D1D97C49A9E8F1 CRC64;
     MSVSAAPAIP QYSVSDYMKF ALAGAIGCGS THSSMVPIDV VKTRIQLEPT VYNKGMVGSF
     KQIIAGEGAG ALLTGFGPTL LGYSIQGAFK FGGYEVFKKF FIDNLGYDTA SRYKNSVYMG
     SAAMAEFLAD IALCPLEATR IRLVSQPQFA NGLVGGFSRI LKEEGIGSFY SGFTPILFKQ
     IPYNIAKFLV FERASEFYYG FAGPKEKLSS TSTTLLNLLS GLTAGLAAAI VSQPADTLLS
     KVNKTKKAPG QSTVGLLAQL AKQLGFFGSF AGLPTRLVMV GTLTSLQFGI YGSLKSTLGC
     PPTIEIGGGG H
 
 
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